Formation of Supramolecular Nanostructures through in Situ Self‐Assembly and Post‐Assembly Modification of a Biocatalytically Constructed Dipeptide Hydrazide**

Abstract

Aqueous self-assembly of short peptides has attracted growing attention for the construction of supramolecular materials for various bioapplications. Herein, we describe how the thermolysin-assisted biocatalytic construction of a dipeptide hydrazide from an N-protected amino acid and an amino acid hydrazide leads to the formation of thermally stable supramolecular hydrogels. In addition, we demonstrate the post-assembly modification of the supramolecular architectures constructed in situ tethering hydrazide groups as a chemical handle by means of fluorescence imaging.

Peptide-based assembled nanostructures that can direct cellular responses

“…Among these, the diphenylalanine peptide (L-Phe-L-Phe; FF) is perhaps the most famous and also the core recognition motif of the Alzheimer's β-amyloid peptide [152,153]. Many studies indicated that this peptide and its derivatives can self-assemble into highly ordered nanostructures such as NPs and nanoribbons [154,155], or nanoscale matrices such as hydrogels [15]. In the FF dipeptide system, the main driving force of the structure self-assembly is the hydrophobic interaction and the π-π interaction.…”